COP9 signalosome components play a role in the mating pheromone response of S. cerevisiae

Maytal-Kivity, V.; Piran, Ron; Pick, E.; Hofmann, K.; Glickman, Michael S.

doi:10.1038/sj.embor.embor850

Cited by 27 publications

(48 citation statements)

References 21 publications

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“…In another example, we predicted that Csn12 was not a component of the COP9 signalosome, which is involved in deneddylation (27). Consistent with this, Maytal-Kivity et al (64) demonstrated that Csn12 is the only component of this complex that is not required for the deneddylation activity. Furthermore we found that Csn12, but not other signalosome subunits, is required for efficient mRNA splicing at a number of genes in budding yeast, 4 suggesting that Csn12 plays multiple cellular roles and may not be an integral member of the complex.…”

Section: Contribution Of Each Data Source For Predictingsupporting

confidence: 58%

A Complex-based Reconstruction of the Saccharomyces cerevisiae Interactome

Wang

Kakaradov

Collins

et al. 2009

Molecular & Cellular Proteomics

102

117

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Most cellular processes are performed by proteomic units that interact with each other. These units are often stoichiometrically stable complexes comprised of several proteins. To obtain a faithful view of the protein interactome we must view it in terms of these basic units (complexes and proteins) and the interactions between them. This study makes two contributions toward this goal. First, it provides a new algorithm for reconstruction of stable complexes from a variety of heterogeneous biological assays; our approach combines state-of-the-art machine learning methods with a novel hierarchical clustering algorithm that allows clusters to overlap. We demonstrate that our approach constructs over 40% more known complexes than other recent methods and that the complexes it produces are more biologically coherent even compared with the reference set. We provide experimental support for some of our novel predictions, identifying both a new complex involved in nutrient starvation and a new component of the eisosome complex. Second, we provide a high accuracy algorithm for the novel problem of predicting transient interactions involving complexes. We show that our complex level network, which we call ComplexNet, provides novel insights regarding the protein-protein interaction network. In particular, we reinterpret the finding that "hubs" in the network are enriched for being essential, showing instead that essential proteins tend to be clustered together in essential complexes and that these essential complexes tend to be large. Biological processes exhibit a hierarchical structure in which the basic working units, proteins, physically associate to form stoichiometrically stable complexes. Complexes interact with individual proteins or other complexes to form functional modules and pathways that carry out most cellular processes. Such higher level interactions are more transient than those within complexes and are highly dependent on temporal and spatial context. The function of each protein or complex depends on its interaction partners. Therefore, a faithful reconstruction of the entire set of complexes in the cell is essential to identifying the function of individual proteins and complexes as well as serving as a building block for understanding the higher level organization of the cell, such as the interactions of complexes and proteins within cellular pathways. Here we describe a novel method for reconstruction of complexes from a variety of biological assays and a method for predicting the network of interactions relating these core cellular units (complexes and proteins).Our reconstruction effort focuses on the yeast Saccharomyces cerevisiae. Yeast serves as the prototypical case study for the reconstruction of protein-protein interaction networks. Moreover the yeast complexes often have conserved orthologs in other organisms, including human, and are of interest in their own right. Several studies (1-4) using a variety of assays have generated high throughput data that directly measure protein-protein inte...

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Section: Contribution Of Each Data Source For Predictingsupporting

confidence: 58%

A Complex-based Reconstruction of the Saccharomyces cerevisiae Interactome

Wang

Kakaradov

Collins

et al. 2009

Molecular & Cellular Proteomics

102

117

View full text Add to dashboard Cite

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“…The budding yeast Saccharomyces cerevisiae possesses an alternative CSN complex. This includes as the only significantly conserved subunit the homolog of Csn5 [18]. Csn5 is the intrinsic CSN enzyme activity including MPN and a JAMM domain for a metalloprotease activity.…”

Section: Csn Organisation and Intrinsic Functionmentioning

confidence: 99%

Fungal development and the COP9 signalosome

Braus

Irniger

Bayram

2010

Current Opinion in Microbiology

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The conserved COP9 signalosome (CSN) multiprotein complex is located at the interface between cellular signaling, protein modification, life span and the development of multicellular organisms. CSN is required for light-controlled responses in filamentous fungi. This includes the circadian rhythm of Neurospora crassa or the repression of sexual development by light in Aspergillus nidulans. In contrast to plants and animals, CSN is not essential for fungal viability. Therefore fungi are suitable models to study CSN composition, activity and cellular functions and its role in light controlled development.

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“…The deneddylation activity resides within CSN subunit CSN5, which to date is the only CSN subunit with a known biochemical activity. CSN5 has an interesting feature in that it is present in all eukaryotes not only as a subunit of CSN but also as a monomer (Freilich et al, 1999;Mundt et al, 1999Mundt et al, , 2002Maytal-Kivity et al, 2002;Oron et al, 2002;Dohmann et al, 2005). Interestingly, although csn subunit mutants typically lack the residual CSN complex and frequently also the residual CSN subunits, the CSN5 monomer is always maintained in these mutants (with the obvious exception of csn5 mutants).…”

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confidence: 99%

Auxin Responses in Mutants of the Arabidopsis CONSTITUTIVE PHOTOMORPHOGENIC9 Signalosome

et al. 2008

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The CONSTITUTIVE PHOTOMORPHOGENIC9 (COP9) signalosome (CSN) is an evolutionarily conserved multiprotein complex that interacts with cullin-RING type E3 ubiquitin ligases (CRLs). CSN subunit 5 (CSN5), which, when incorporated into CSN, can deconjugate the NEDD8 modification from the cullin subunit of CRLs, is essential for CSN's role in controlling CRL activity. Whether the CSN5 monomer, which is maintained in csn mutants such as csn3 or csn4, has a functional role, remains to be established. We performed a comparative gene expression-profiling experiment with Arabidopsis (Arabidopsis thaliana) csn3, csn4, and csn5 mutants, and we show here that these mutants cannot be distinguished at the transcriptional level. Furthermore, we show that csn3 csn5 mutants are morphologically indistinguishable from csn3 or csn5 mutants. Taken together, these data suggest that the CSN5 monomer does not have a function that leads to transcriptional or morphological changes in the csn mutants. We further examined auxin responses in csn mutants. Whereas CSN had previously been shown to be required for the auxin response-regulatory E3 complexes, specifically SCF TIR1 , the csn mutant phenotype suggests that CSN is not essential for auxin responses. We present physiological and genetic data that indicate that auxin responses are indeed only partially impaired in csn mutants and that this is not the result of maternally contributed CSN. Finally, we discuss these findings in the context of the current understanding of the role of neddylation and CSN-mediated deneddylation for CRL activity.

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COP9 signalosome components play a role in the mating pheromone response of S. cerevisiae

Abstract: CORRECTIONIn the December 2002 issue of EMBO reports, we published an error about the name and contribution of one of the authors, Elah Pick. The second footnote should have read, "V. Maytal-Kivity, R. Piran and E. Pick contributed equally to this work."

Cited by 27 publications

References 21 publications

A Complex-based Reconstruction of the Saccharomyces cerevisiae Interactome

A Complex-based Reconstruction of the Saccharomyces cerevisiae Interactome

Fungal development and the COP9 signalosome

Auxin Responses in Mutants of the Arabidopsis CONSTITUTIVE PHOTOMORPHOGENIC9 Signalosome

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